Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha.

@article{Elkins2003StructureOF,
  title={Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha.},
  author={Jonathan M Elkins and Kirsty S. Hewitson and Luke A. McNeill and Jurgen F Seibel and Imre Schlemminger and Christopher W Pugh and Peter J Ratcliffe and Christopher J. Schofield},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 3},
  pages={1802-6}
}
The activity of the transcription factor hypoxia-inducible factor (HIF) is regulated by oxygen-dependent hydroxylation. Under normoxic conditions, hydroxylation of proline residues triggers destruction of its alpha-subunit while hydroxylation of Asn(803) in the C-terminal transactivation domain of HIF-1 alpha (CAD) prevents its interaction with p300. Here we report crystal structures of the asparagine hydroxylase (factor-inhibiting HIF, FIH) complexed with Fe((II)), 2-oxoglutarate cosubstrate… CONTINUE READING

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